Manganese in PDB 4hx4: Structure of Mntr Mutant E11K Complexed with MN2+

The structure of Structure of Mntr Mutant E11K Complexed with MN2+, PDB code: 4hx4 was solved by A.Glasfeld, A.Mcguire, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.33 / 1.65
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.427, 46.081, 74.892, 90.00, 92.96, 90.00
R / Rfree (%)	23.4 / 26.4

The binding sites of Manganese atom in the Structure of Mntr Mutant E11K Complexed with MN2+ (pdb code 4hx4). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of Mntr Mutant E11K Complexed with MN2+, PDB code: 4hx4:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Structure of Mntr Mutant E11K Complexed with MN2+


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Mntr Mutant E11K Complexed with MN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:31.0 occ:1.00 O A:HOH309 2.1 25.4 1.0 OE1 A:GLU99 2.2 30.7 1.0 OE2 A:GLU102 2.2 28.0 1.0 O A:GLU99 2.4 23.8 1.0 NE2 A:HIS103 2.4 27.5 1.0 OD2 A:ASP8 2.4 35.5 1.0 CD A:GLU99 3.3 29.5 1.0 CD A:GLU102 3.3 27.6 1.0 C A:GLU99 3.3 24.8 1.0 CD2 A:HIS103 3.4 27.0 1.0 CG A:ASP8 3.4 36.6 1.0 CE1 A:HIS103 3.4 27.9 1.0 OD1 A:ASP8 3.5 38.7 1.0 CA A:GLU99 3.5 24.7 1.0 CG A:GLU102 3.7 25.9 1.0 CB A:GLU99 3.9 26.6 1.0 OE2 A:GLU99 4.0 30.4 1.0 O A:HOH346 4.2 36.5 1.0 CG A:GLU99 4.2 28.0 1.0 NZ A:LYS11 4.3 36.8 1.0 OE1 A:GLU102 4.4 29.4 1.0 ND1 A:HIS103 4.5 27.5 1.0 CG A:HIS103 4.5 27.0 1.0 N A:GLY100 4.5 24.3 1.0 CB A:ASP8 4.8 35.1 1.0 N A:GLU99 4.9 22.9 1.0 CE A:LYS11 4.9 34.6 1.0

Manganese binding site 2 out of 2 in the Structure of Mntr Mutant E11K Complexed with MN2+


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of Mntr Mutant E11K Complexed with MN2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn201 b:29.4 occ:1.00 OE2 B:GLU102 2.2 22.6 1.0 O B:HOH338 2.3 29.7 1.0 OE1 B:GLU99 2.3 26.1 1.0 OD2 B:ASP8 2.4 31.5 1.0 O B:GLU99 2.4 20.5 1.0 NE2 B:HIS103 2.4 26.4 1.0 CD B:GLU102 3.3 22.0 1.0 CD2 B:HIS103 3.3 25.9 1.0 C B:GLU99 3.3 21.1 1.0 CE1 B:HIS103 3.3 26.3 1.0 CG B:ASP8 3.4 32.6 1.0 CD B:GLU99 3.4 24.9 1.0 CA B:GLU99 3.6 20.8 1.0 OD1 B:ASP8 3.6 34.3 1.0 CG B:GLU102 3.8 20.4 1.0 CB B:GLU99 4.0 22.6 1.0 OE2 B:GLU99 4.2 25.3 1.0 O B:HOH327 4.3 36.3 1.0 CG B:GLU99 4.3 23.6 1.0 OE1 B:GLU102 4.3 22.2 1.0 ND1 B:HIS103 4.4 26.4 1.0 CG B:HIS103 4.4 26.2 1.0 N B:GLY100 4.5 19.9 1.0 NZ B:LYS11 4.6 32.2 1.0 CB B:ASP8 4.7 31.1 1.0 N B:GLU99 5.0 19.6 1.0

A.M.Mcguire, B.J.Cuthbert, Z.Ma, K.D.Grauer-Gray, M.Brunjes Brophy, K.A.Spear, S.Soonsanga, J.I.Kliegman, S.L.Griner, J.D.Helmann, A.Glasfeld. Roles of the A and C Sites in the Manganese-Specific Activation of Mntr. Biochemistry V. 52 701 2013.
ISSN: ISSN 0006-2960
PubMed: 23298157
DOI: 10.1021/BI301550T